Thermo Fisher Scientific Human IGF-I LR3 Recombinant Protein, PeproTech

Applications

Tested Dilution

Publications

Functional Assay (Functional)

Assay-dependent

-

In vitro Assay (IV)

-

View 3 publications 3 publications

Product Specifications

Species

Human

Published species

Human

Expression System

E. coli

Amino acid sequence

MFPAMPLSSL FVNGPRTLCG AELVDALQFV CGDRGFYFNK PTGYGSSSRR APQTGIVDEC CFRSCDLRRL EMYCAPLKPA KSA

Molecular weight

9.1 kDa

Class

Recombinant

Type

Protein

Purity

≥ 98% by SDS-PAGE gel and HPLC analyses.

Endotoxin concentration

<1 EU/µg

Activity

The ED50 was determined by a cell proliferation assay using FDC-P1 cells is ≤ 2.0 ng/ml, corresponding to a specific activity of ≥ 5 x 10^5 units/mg.

Conjugate

Unconjugated Unconjugated Unconjugated

Form

Lyophilized

Purification

purified

Contains

no preservative

Storage conditions

-20°C

Shipping conditions

Ambient

Product Specific Information

Recombinant Recombinant Human IGF-I LR3 is a 9.1 kDa, single, non-glycosylated polypeptide chain containing 83 amino acid residues.

This product is shipped at ambient temperature. For storage, handling and reconstitution information, please see the lot-specific Certificate of Analysis

Target Information

The IGFs are mitogenic, polypeptide growth factors that stimulate the proliferation and survival of various cell types, including muscle, bone, and cartilage tissue in vitro. IGFs are predominantly produced by the liver, although a variety of tissues produce the IGFs at distinctive times. The IGFs belong to the Insulin gene family, which also contains insulin and relaxin. The IGFs are similar to insulin by structure and function, but have a much higher growth-promoting activity than insulin. IGF-II expression is influenced by placenta lactogen, while IGF-I expression is regulated by growth hormone. Both IGF-I and IGF-II signal through the tyrosine kinase type I receptor (IGF-IR), but IGF-II can also signal through the IGF-II/Mannose-6-phosphate receptor. Mature IGFs are generated by proteolytic processing of inactive precursor proteins, which contain N-terminal and C-terminal propeptide regions. Recombinant human IGF-I and IGF-II are globular proteins containing 70 and 67 amino acids, respectively, and 3 intra-molecular disulfide bonds. IGF-I LR3 is a recombinant analog of human IGF-I comprised of the complete IGF-I sequence, with an Arginine substitution for the third position Glutamic acid, and a 13 amino acid length N terminus peptide extension. Specifically engineered for higher biological potency in vitro, IGF-I LR3 has an increased half-life and a binding aversion to native proteins within the body that make it ideal for both research and large-scale culturing.

For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.